| Structural highlights
2vbd is a 1 chain structure with sequence from Emericella nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | ,
| | Related: | 1hb1, 1ips, 1oc1, 1w04, 1w05, 1w3v, 2bjs, 2jb4, 2vau, 1bk0, 1blz, 1hb2, 1hb3, 1hb4, 1obn, 1odm, 1odn, 1qiq, 1qje, 1qjf, 1uzw, 1w03, 1w06, 1w3x, 2bu9, 2ivi, 2ivj, 2vbb |
| Activity: | Isopenicillin-N synthase, with EC number 1.21.3.1 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Isopenicillin N synthase (IPNS) is a non-heme iron(ii) oxidase, which catalyses the biosynthesis of isopenicillin N (IPN) from the tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine (lld-ACV) in a remarkable oxidative bicyclisation reaction. The natural substrate for IPNS is the lld-configured tripeptide. lll-ACV is not turned over by the enzyme, but inhibits turnover of the lld-tripeptide. The mechanism by which this inhibition takes place is not fully understood. Recent studies have employed a range of lld-configured depsipeptide substrate analogues in crystallographic studies to probe events preceding beta-lactam closure in the IPNS reaction cycle. Herein, we report the first crystal structure of IPNS in complex with an lll-configured depsipeptide analogue, delta-l-alpha-aminoadipoyl-l-cysteine (1-(R)-carboxy-2-thiomethyl)ethyl ester (lll-ACOmC). This report describes the crystal structure of the IPNS:Fe(ii):lll-ACOmC complex to 2.0 A resolution, and discusses attempts to oxygenate this complex at high pressure in order to probe the mechanism by which lll-configured substrates inhibit IPNS catalysis.
The crystal structure of an LLL-configured depsipeptide substrate analogue bound to isopenicillin N synthase.,Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ Org Biomol Chem. 2010 Jan 7;8(1):122-7. doi: 10.1039/b910170e. Epub 2009 Oct 29. PMID:20024142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ. The crystal structure of an LLL-configured depsipeptide substrate analogue bound to isopenicillin N synthase. Org Biomol Chem. 2010 Jan 7;8(1):122-7. doi: 10.1039/b910170e. Epub 2009 Oct 29. PMID:20024142 doi:http://dx.doi.org/10.1039/b910170e
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